中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Membrane attachment and structure models of lipid storage droplet protein 1

文献类型:期刊论文

作者Lin, Penghui1; Chen, Xiao2; Moktan, Hem1; Arrese, Estela L.2; Duan, Lian1; Wang, Liying1,3; Soulages, Jose L.2; Zhou, Donghua H.1
刊名BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
出版日期2014-03-01
卷号1838期号:3页码:874-881
关键词Lipid storage droplet protein Triglyceride lipolysis Proton spin diffusion Magic-angle spinning Solid-state NMR MD simulation
英文摘要Neutral lipid triglycerides, a main reserve for fat and energy, are stored in organelles called lipid droplets. The storage and release of triglycerides are actively regulated by several proteins specific to the droplet surface, one of which in insects is PLIN1. PLIN1 plays a key role in the activation of triglyceride hydrolysis upon phosphorylation. However, the structure of PLIN1 and its relation to functions remain elusive due to its insolubility and crystallization difficulty. Here we report the first solid-state NMR study on the Drosophila melanogaster PLIN1 in combination with molecular dynamics simulation to show the structural basis for its lipid droplet attachment. NMR spin diffusion experiments were consistent with the predicted membrane attachment motif of PLIN1. The data indicated that PLIN1 has close contact with the terminal methyl groups of the phospholipid acyl chains. Structure models for the membrane attachment motif were generated based on hydrophobicity analysis and NMR membrane insertion depth information. Simulated NMR spectra from a trans-model agreed with experimental spectra. In this model, lipids from the bottom leaflet were very close to the surface in the region enclosed by membrane attachment motif. This may imply that in real lipid droplet, triglyceride molecules might be brought close to the surface by the same mechanism, ready to leave the droplet in the event of lipolysis. Juxtaposition of triglyceride lipase structure to the trans-model suggested a possible interaction of a conserved segment with the lipase by electrostatic interactions, opening the lipase lid to expose the catalytic center. (C) 2013 Elsevier B.V. All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemistry & Molecular Biology ; Biophysics
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics
关键词[WOS]SOLID-STATE NMR ; MOLECULAR-DYNAMICS METHOD ; FAT-BODY ; DROSOPHILA-MELANOGASTER ; DISCOIDAL LIPOPROTEINS ; CONFORMATIONAL-CHANGE ; APOLIPOPHORIN-III ; SPIN-DIFFUSION ; MANDUCA-SEXTA ; PAT-FAMILY
收录类别SCI
语种英语
WOS记录号WOS:000331661800017
公开日期2015-07-14
源URL[http://ir.wipm.ac.cn/handle/112942/1368]  
专题武汉物理与数学研究所_高技术创新与发展中心
作者单位1.Oklahoma State Univ, Dept Phys, Stillwater, OK 74078 USA
2.Oklahoma State Univ, Dept Biochem & Mol Biol, Stillwater, OK 74078 USA
3.Chinese Acad Sci, Wuhan Ctr Magnet Resonance, Wuhan Inst Phys & Math,Key Lab Magnet Resonance B, State Key Lab Magnet Resonance & Atom Mol Phys, Wuhan 430071, Peoples R China
推荐引用方式
GB/T 7714
Lin, Penghui,Chen, Xiao,Moktan, Hem,et al. Membrane attachment and structure models of lipid storage droplet protein 1[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,2014,1838(3):874-881.
APA Lin, Penghui.,Chen, Xiao.,Moktan, Hem.,Arrese, Estela L..,Duan, Lian.,...&Zhou, Donghua H..(2014).Membrane attachment and structure models of lipid storage droplet protein 1.BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,1838(3),874-881.
MLA Lin, Penghui,et al."Membrane attachment and structure models of lipid storage droplet protein 1".BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 1838.3(2014):874-881.

入库方式: OAI收割

来源:武汉物理与数学研究所

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